PP2A-B55 promotes nuclear envelope reformation after mitosis in Drosophila

• DOI: 10.1083/jcb.201804018
• Publication Date: 2018-10-11T13:20:08Z
• Authors: Haytham Mehsen; Vincent Boudreau; Damien Garrido; Mohammed Bourouh; Myreille Larouche; Paul S. Maddox; Andrew Swan; Vincent Archambault
• Keywords: Mitotic exit; Meiosis II; Interphase; Dephosphorylation

As a dividing cell exits mitosis and daughter cells enter interphase, many proteins must be dephosphorylated. The protein phosphatase 2A (PP2A) with its B55 regulatory subunit plays crucial role in this transition, but the identity of substrates how their dephosphorylation promotes mitotic exit are largely unknown. We conducted maternal-effect screen Drosophila melanogaster to identify genes that function PP2A-B55/Tws cycle. found eggs receive reduced levels Tws components nuclear envelope (NE) often fail development, concomitant NE defects following meiosis syncytial mitoses. Our mechanistic studies using indicate PP2A-Tws reformation (NER) during by dephosphorylating BAF suggests targets additional components, including Lamin Nup107. This work establishes as powerful model further dissect molecular mechanisms NER roles completion mitosis.